[English] 日本語
Yorodumi
- PDB-8i9m: The RAGE and HMGB1 complex -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8i9m
TitleThe RAGE and HMGB1 complex
Components
  • Advanced glycosylation end product-specific receptor
  • High mobility group protein B1
KeywordsIMMUNE SYSTEM / RAGE / HMGB1 / Inflammation
Function / homology
Function and homology information


regulation of restriction endodeoxyribonuclease activity / regulation of tolerance induction / positive regulation of mismatch repair / regulation of T cell mediated immune response to tumor cell / regulation of CD4-positive, alpha-beta T cell activation / negative regulation of blood circulation / negative regulation of apoptotic cell clearance / advanced glycation end-product receptor activity / positive regulation of endothelin production / negative regulation of RNA polymerase II transcription preinitiation complex assembly ...regulation of restriction endodeoxyribonuclease activity / regulation of tolerance induction / positive regulation of mismatch repair / regulation of T cell mediated immune response to tumor cell / regulation of CD4-positive, alpha-beta T cell activation / negative regulation of blood circulation / negative regulation of apoptotic cell clearance / advanced glycation end-product receptor activity / positive regulation of endothelin production / negative regulation of RNA polymerase II transcription preinitiation complex assembly / DNA geometric change / regulation of T cell mediated cytotoxicity / myeloid dendritic cell activation / glucose mediated signaling pathway / T-helper 1 cell activation / negative regulation of long-term synaptic depression / C-X-C chemokine binding / T-helper 1 cell differentiation / positive regulation of monocyte extravasation / positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process / positive regulation of dendritic cell differentiation / negative regulation of CD4-positive, alpha-beta T cell differentiation / regulation of p38MAPK cascade / positive regulation of toll-like receptor 9 signaling pathway / neutrophil clearance / regulation of non-canonical NF-kappaB signal transduction / positive regulation of DNA ligation / positive regulation of interleukin-1 production / RAGE receptor binding / Regulation of TLR by endogenous ligand / scavenger receptor activity / alphav-beta3 integrin-HMGB1 complex / induction of positive chemotaxis / bubble DNA binding / V(D)J recombination / transcytosis / protein localization to membrane / Apoptosis induced DNA fragmentation / positive regulation of monocyte chemotactic protein-1 production / inflammatory response to antigenic stimulus / positive regulation of chemokine (C-X-C motif) ligand 2 production / positive regulation of monocyte chemotaxis / MyD88 deficiency (TLR2/4) / supercoiled DNA binding / positive regulation of heterotypic cell-cell adhesion / S100 protein binding / apoptotic cell clearance / regulation of long-term synaptic potentiation / regulation of spontaneous synaptic transmission / dendritic cell chemotaxis / laminin receptor activity / positive regulation of p38MAPK cascade / DNA binding, bending / positive regulation of vascular endothelial cell proliferation / IRAK4 deficiency (TLR2/4) / MyD88:MAL(TIRAP) cascade initiated on plasma membrane / negative regulation of interleukin-10 production / positive regulation of activated T cell proliferation / phosphatidylserine binding / chemoattractant activity / positive regulation of cysteine-type endopeptidase activity involved in apoptotic process / response to amyloid-beta / DNA topological change / TRAF6 mediated NF-kB activation / positive regulation of interleukin-10 production / Advanced glycosylation endproduct receptor signaling / negative regulation of blood vessel endothelial cell migration / negative regulation of type II interferon production / transport across blood-brain barrier / endoplasmic reticulum-Golgi intermediate compartment / negative regulation of long-term synaptic potentiation / positive regulation of blood vessel endothelial cell migration / positive regulation of DNA binding / Pyroptosis / positive regulation of autophagy / heterochromatin formation / DNA polymerase binding / four-way junction DNA binding / positive regulation of chemokine production / condensed chromosome / positive regulation of interleukin-12 production / activation of innate immune response / transcription repressor complex / positive regulation of interleukin-1 beta production / cytokine activity / positive regulation of interleukin-8 production / astrocyte activation / lipopolysaccharide binding / positive regulation of JNK cascade / microglial cell activation / TAK1-dependent IKK and NF-kappa-B activation / regulation of synaptic plasticity / fibrillar center / autophagy / response to wounding / double-strand break repair via nonhomologous end joining / positive regulation of non-canonical NF-kappaB signal transduction / cellular response to amyloid-beta / transmembrane signaling receptor activity / transcription corepressor activity
Similarity search - Function
HMG box A DNA-binding domain, conserved site / HMG box A DNA-binding domain signature. / HMG-box domain / CD80-like, immunoglobulin C2-set / CD80-like C2-set immunoglobulin domain / HMG (high mobility group) box / HMG boxes A and B DNA-binding domains profile. / high mobility group / High mobility group box domain / High mobility group box domain superfamily ...HMG box A DNA-binding domain, conserved site / HMG box A DNA-binding domain signature. / HMG-box domain / CD80-like, immunoglobulin C2-set / CD80-like C2-set immunoglobulin domain / HMG (high mobility group) box / HMG boxes A and B DNA-binding domains profile. / high mobility group / High mobility group box domain / High mobility group box domain superfamily / Immunoglobulin / Immunoglobulin domain / Immunoglobulin domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
High mobility group protein B1 / Advanced glycosylation end product-specific receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 5.19 Å
AuthorsHan, C.W. / Kim, H.J.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: To Be Published
Title: The RAGE and HMGB1 complex
Authors: Han, C.W. / Kim, H.J.
History
DepositionFeb 7, 2023Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Feb 14, 2024Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: High mobility group protein B1
B: Advanced glycosylation end product-specific receptor


Theoretical massNumber of molelcules
Total (without water)31,6592
Polymers31,6592
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, 1 copy of chain A 1 copy of chain B
TypeNameSymmetry operationNumber
identity operation1_5551

-
Components

#1: Protein High mobility group protein B1 / High mobility group protein 1 / HMG-1


Mass: 8590.859 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HMGB1, HMG1 / Production host: Escherichia coli (E. coli) / References: UniProt: P09429
#2: Protein Advanced glycosylation end product-specific receptor / Receptor for advanced glycosylation end products


Mass: 23068.414 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: AGER, RAGE / Production host: Escherichia coli (E. coli) / References: UniProt: Q15109

-
Experimental details

-
Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

-
Sample preparation

ComponentName: The RAGE and HMGB1 complex / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Molecular weightValue: 0.50 MDa / Experimental value: YES
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: GOLD / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R2/2
VitrificationCryogen name: NITROGEN

-
Electron microscopy imaging

MicroscopyModel: TFS GLACIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM
Electron lensMode: DARK FIELD / Nominal defocus max: 3000 nm / Nominal defocus min: 1800 nm
Image recordingElectron dose: 39.99 e/Å2 / Film or detector model: FEI FALCON III (4k x 4k)

-
Processing

Software
NameVersionClassification
phenix.real_space_refine1.14_3260refinement
PHENIX1.14_3260refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 5.19 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 121467 / Symmetry type: POINT
RefinementStereochemistry target values: CDL v1.2
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.01452289
ELECTRON MICROSCOPYf_angle_d2.31213103
ELECTRON MICROSCOPYf_chiral_restr0.1215324
ELECTRON MICROSCOPYf_plane_restr0.0181409
ELECTRON MICROSCOPYf_dihedral_angle_d13.46551408

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbjlvh1.pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more